|
Name |
Accession |
Description |
Interval |
E-value |
| pgm |
TIGR01132 |
phosphoglucomutase, alpha-D-glucose phosphate-specific; This enzyme interconverts ... |
2-544 |
0e+00 |
|
phosphoglucomutase, alpha-D-glucose phosphate-specific; This enzyme interconverts alpha-D-glucose-1-P and alpha-D-glucose-6-P. [Energy metabolism, Sugars]
Pssm-ID: 273459 Cd Length: 543 Bit Score: 1054.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 2 AIDKRAGQPAQQSDLINVAQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAGRHNFNEQHILAIAQAIAENRAKNGITGPC 81
Cdd:TIGR01132 1 AIHPRAGQPAQQEDLINVAQLVAQYYVLQPEAGNAAHAVKFGTSGHRGSALRGTFNEPHILAIAQAIAEYRAAQGITGPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 82 YVGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPN 161
Cdd:TIGR01132 81 YIGKDTHALSEPAFISVLEVLAANGVEVIVQENNGFTPTPAVSHAILTHNKKGEPLADGIVITPSHNPPEDGGIKYNPPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 162 GGPADTNVTKVVENRANELLAAGLQGVKRISLDAALASGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGI 241
Cdd:TIGR01132 161 GGPADTEATQAIEDRANALLANGLKGVKRLPLAQALASGTVKAHDLVQPYVDGLADIVDMAAIQKAGLRLGVDPLGGSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 242 EYWKRIGEHYKLDLTIVNDQVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTPAGLMNP 321
Cdd:TIGR01132 241 DYWKRIAEKYNLNLTLVNPQVDPTFRFMTLDKDGKIRMDCSSPYAMAGLLALRDKYDLAFGNDPDYDRHGIVTPAGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 322 NHYLAVAINYLFQHRPQWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 401
Cdd:TIGR01132 321 NHYLAVAINYLFQHRPQWGGDVAVGKTLVSSAMIDRVVADLGRQLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 402 GTPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNELAERFGAPSYNRLQASATSAQKAALSKLSPEMVSADTLAGDPITAR 481
Cdd:TIGR01132 401 GTPWSTDKDGIIMCLLAAEITAVTGKNPQQHYNELAAKFGAPSYNRIQAPATSAQKARLKKLSPEMVSATTLAGDPITAR 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180591 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEEHRKLIEKEAVEIVSEVLK 544
Cdd:TIGR01132 481 LTAAPGNGAAIGGLKVTTDNGWFAARPSGTEDVYKIYCESFKGEEHLKQIEKEAVEIVSEVLK 543
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
3-544 |
0e+00 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 1041.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 3 IDKRAGQPAQQSDLINVAQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAGRHNFNEQHILAIAQAIAENRAKNGITGPCY 82
Cdd:PRK07564 1 IHPRAGQPAQPSDLINVPRLVSAYYTLKPDPTNPFQDVKFGTSGHRGSSLQPSFNENHILAIFQAICEYRGKQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 83 VGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:PRK07564 81 VGGDTHALSEPAIQSALEVLAANGVGVVIVGRGGYTPTPAVSHAILKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 163 GPADTNVTKVVENRANELLAAGLQGVKRISLDAALASGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIE 242
Cdd:PRK07564 161 GPADTDVTDAIEARANELLAYGLKGVKRIPLDRALASMTVEVIDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 243 YWKRIGEHYKLDLTIVNDQVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTPAGLMNPN 322
Cdd:PRK07564 241 YWKAIAERYGLDLTVVNAPVDPTFNFMPLDDDGKIRMDCSSPYAMAGLLALKDAFDLAFANDPDGDRHGIVTPGGLMNPN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 323 HYLAVAINYLFQHRPQWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDG 402
Cdd:PRK07564 321 HYLAVAIAYLFHHRPGWRAGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRRDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 403 TPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNELAERFGAPSYNRLQASATSAQKAALSKLSPEMVSADTLAGDPITARL 482
Cdd:PRK07564 401 SVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWARFGRPYYSRHDAPATPEQKAALRKLSPELVGATELAGDPIDASL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180591 483 TAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEEHRKLIEKEAVEIVSEVLK 544
Cdd:PRK07564 481 TEAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIQKEAQEIVADLIA 542
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
20-539 |
0e+00 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100094 [Multi-domain] Cd Length: 522 Bit Score: 1039.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 20 AQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAGRHNFNEQHILAIAQAIAENRAKNGITGPCYVGKDTHALSEPAFISVL 99
Cdd:cd05801 1 PRLITAYYTLKPDPSNPAQRVAFGTSGHRGSSLKGSFNEAHILAISQAICDYRKSQGITGPLFLGKDTHALSEPAFISAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 100 EVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKG-GPLADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRAN 178
Cdd:cd05801 81 EVLAANGVEVIIQQNDGYTPTPVISHAILTYNRGRtEGLADGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 179 ELLAAGLQGVKRISLDAALASGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIGEHYKLDLTIV 258
Cdd:cd05801 161 ALLANGLKGVKRIPLEAALASGYTHRHDFVTPYVADLGNVIDMDAIRKSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 259 NDQVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTP-AGLMNPNHYLAVAINYLFQHRP 337
Cdd:cd05801 241 NPKVDPTFRFMTLDHDGKIRMDCSSPYAMAGLLKLKDKFDLAFANDPDADRHGIVTPsAGLMNPNHYLSVAIDYLFTHRP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 338 QWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDGTPWSTDKDGIIMCLL 417
Cdd:cd05801 321 LWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDGTVWTTDKDGIIMCLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 418 AAEITAVTGKNPQEHYNELAERFGAPSYNRLQASATSAQKAALSKLSPEMVSADTLAGDPITARLTAAPGNGASIGGLKV 497
Cdd:cd05801 401 AAEILAVTGKDPGQLYQELTERFGEPYYARIDAPATPEQKARLKKLSPEQVTATELAGDPILAKLTRAPGNGASIGGLKV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 505180591 498 MTDNGWFAARPSGTEDAYKIYCESFLGEEHRKLIEKEAVEIV 539
Cdd:cd05801 481 TTANGWFAARPSGTEDVYKIYAESFLSEEHLKKIQKEAQEIV 522
|
|
| Pgm |
COG0033 |
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism]; |
3-544 |
0e+00 |
|
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 439803 Cd Length: 544 Bit Score: 1013.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 3 IDKRAGQPAQQSDLINVAQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAGRHNFNEQHILAIAQAIAENRAKNGITGPCY 82
Cdd:COG0033 1 LHPRAGQPAPPSDLIDVPRLVSAYYTIKPDPTTPFQDVKFGTSGHRGSSLKGSFNEPHILAITQAIFDYRKAQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 83 VGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:COG0033 81 LGGDTHALSEPAIQTALEVLAANGVGVVIVGQGGYTPTPAVSHAILKYNRGTSGAADGIVLTPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 163 GPADTNVTKVVENRANELLAAGLQGVKRISLDAALASGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIE 242
Cdd:COG0033 161 GPADEDVTDAIEARANEILEYGLADVKRVPLDRAGTAMTVEVIDPVADYVELLESVFDFDAIRAAGFRIGFDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 243 YWKRIGEHYKLDLTIVNDQVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTP-AGLMNP 321
Cdd:COG0033 241 YWKAIAERYGLDLTVVNGVPDPDFRFMTLDWDGGIRMDPSSPYAMASLIAGKDAPDFAAANDGDGDRHGIVTPrGGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 322 NHYLAVAINYLFQHRPQWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 401
Cdd:COG0033 321 NHYLAVAIAYLFTHRPGWAALAGVGKTMVTSSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGASFLRRD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 402 GTPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNELAERFGAPSYNRLQASATSAQKAALSKLSPEMVSADTLAGDPITAR 481
Cdd:COG0033 401 GSVWTTDKDGLWAVLLAAEILAVTGKSPAEIYRELWARFGRPYYSRHDAEATDEQKARLAKLSGEQVGATTLAGEDIFAY 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180591 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEEHRKLIEKEAVEIVSEVLK 544
Cdd:COG0033 481 LDPAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIDAEAADLVDAALA 543
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
41-539 |
2.10e-106 |
|
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100086 [Multi-domain] Cd Length: 355 Bit Score: 322.77 E-value: 2.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 41 KFGTSGHRGSAGRHnFNEQHILAIAQAIAEnrakngitgpcyvgkdthalsepafisvlevlaangvdvivqenngftpt 120
Cdd:cd03084 1 IFGTSGVRGVVGDD-ITPETAVALGQAIGS-------------------------------------------------- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 121 pavsnailvhnkkggplADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANELLAAGLQGVKrisldaalASG 200
Cdd:cd03084 30 -----------------TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYE--------LGG 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 201 HVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIGEHYKLDLTIVNDQVDQTFrfmhldkdGAIRMD 280
Cdd:cd03084 85 SVKAVDILQRYFEALKKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNF--------GNINPD 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 281 CSSECAMAGLLALRD--KFDLAFANDPDYDRHGIVTP-AGLMNPNHYLAVAINYLFQHrpqWGKDVAVGKTLVSSAMIDR 357
Cdd:cd03084 157 PGSETNLKQLLAVVKaeKADFGVAFDGDADRLIVVDEnGGFLDGDELLALLAVELFLT---FNPRGGVVKTVVSSGALDK 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 358 VVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFdgtpwSTDKDGIIMCLLAAEITAVTGKNPQEHYNELA 437
Cdd:cd03084 234 VAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEF-----HPGRDGISAALLLLEILANLGKSLSELFSELP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 438 erfgAPSYNRLQASatsaqkaalsklspemvsadtlagdpitarltaapgngasigglkvmtdnGWFAARPSGTEDAYKI 517
Cdd:cd03084 309 ----RYYYIRLKVR--------------------------------------------------GWVLVRASGTEPAIRI 334
|
490 500
....*....|....*....|..
gi 505180591 518 YCESFLgEEHRKLIEKEAVEIV 539
Cdd:cd03084 335 YAEADT-QEDVEQIKKEARELV 355
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
40-539 |
2.95e-93 |
|
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.
Pssm-ID: 100093 Cd Length: 461 Bit Score: 292.53 E-value: 2.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 40 VKFGTSGHRGSAGRhNFNEQHILAIAQAIAENRAKNGITGP-CYVGKDTHALSEPAFISVLEVLAANGVDVIVQEnnGFT 118
Cdd:cd05800 1 IKFGTDGWRGIIAE-DFTFENVRRVAQAIADYLKEEGGGGRgVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSD--RPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 119 PTPAVSNAILVHNkkggpLADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANELLAAGLQgvkrisldaALA 198
Cdd:cd05800 78 PTPAVSWAVKKLG-----AAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLE---------ARA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 199 SGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIGEHYKLDLTIVNDQVDQTFrfmhldkdGAIR 278
Cdd:cd05800 144 EGLIETIDPKPDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLF--------GGIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 279 MDCSSEcAMAGLLAL--RDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPQWGkdvAVGKTLVSSAMI 355
Cdd:cd05800 216 PEPIEK-NLGELAEAvkEGGADLGLATDGDADRIGAVDEKGnFLDPNQILALLLDYLLENKGLRG---PVVKTVSTTHLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 356 DRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFdgTPwstDKDGIIMCLLAAEITAVTGKNPQEHYNE 435
Cdd:cd05800 292 DRIAEKHGLPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGH--IP---ERDGILAGLLLLEAVAKTGKPLSELVAE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 436 LAERFGAPSYNRLQASATSAQKAA-LSKLSPEmvSADTLAGDPITARLTaapgngasIGGLKVMTDNG-WFAARPSGTED 513
Cdd:cd05800 367 LEEEYGPSYYDRIDLRLTPAQKEAiLEKLKNE--PPLSIAGGKVDEVNT--------IDGVKLVLEDGsWLLIRPSGTEP 436
|
490 500
....*....|....*....|....*.
gi 505180591 514 AYKIYCESFLGEEHRKLIEkEAVEIV 539
Cdd:cd05800 437 LLRIYAEAPSPEKVEALLD-AGKKLA 461
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-543 |
1.95e-65 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 219.69 E-value: 1.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 42 FGTSGHRGSAGRhNFNEQHILAIAQAIAE---NRAKNGITgpcyVGKDTHALSEPAFISVLEVLAANGVDVIvqeNNGFT 118
Cdd:COG1109 7 FGTDGIRGIVGE-ELTPEFVLKLGRAFGTylkEKGGPKVV----VGRDTRLSSPMLARALAAGLASAGIDVY---DLGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 119 PTPAVSNAILVHNKKGGpladgIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANEllaaglqgvKRISLDAALA 198
Cdd:COG1109 79 PTPALAFAVRHLGADGG-----IMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEK---------EDFRRAEAEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 199 SGHVKE-QDLVQPFIEGLADIVDmAAIQKAGLKLGVDPLGGSGIEYWKRIGEHYKLDLTIVNDQVDQTFRFMHLDKDgai 277
Cdd:COG1109 145 IGKVTRiEDVLEAYIEALKSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPE--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 278 rmdcssECAMAGL--LALRDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPqwGKDVAvgKTLVSSAM 354
Cdd:COG1109 221 ------PENLEDLieAVKETGADLGIAFDGDADRLGVVDEKGrFLDGDQLLALLARYLLEKGP--GGTVV--VTVMSSLA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 355 IDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLrfdgtPWSTDKDGIIMCLLAAEITAVTGKNPQEHYN 434
Cdd:COG1109 291 LEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGGIIFP-----DFVPTDDGILAALLLLELLAKQGKSLSELLA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 435 ELaerfgaPSYNRLQASATSAQKAALSKLSPEMVSADTLAGDPITarltaapgngasIGGLKV-MTDNGWFAARPSGTED 513
Cdd:COG1109 366 EL------PRYPQPEINVRVPDEEKIGAVMEKLREAVEDKEELDT------------IDGVKVdLEDGGWVLVRPSGTEP 427
|
490 500 510
....*....|....*....|....*....|
gi 505180591 514 AYKIYCESFlGEEHRKLIEKEAVEIVSEVL 543
Cdd:COG1109 428 LLRVYAEAK-DEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
320-440 |
7.12e-42 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 146.06 E-value: 7.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 320 NPNHYLAVAINYLFQHRpQWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLR 399
Cdd:pfam02880 1 DGDQILALLAKYLLEQG-KLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 505180591 400 FDgtpwsTDKDGIIMCLLAAEITAVTGKNPQEHYNELAERF 440
Cdd:pfam02880 80 HA-----TTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
40-179 |
2.07e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 142.75 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 40 VKFGTSGHRGSAGRHNFNEQHILAIAQAIAENRAKNGITGPCYVGKDTHALSEPAFISVLEVLAANGVDVIVqenNGFTP 119
Cdd:pfam02878 2 QLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVIL---LGLLP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 120 TPAVSNAILVHNKKGgpladGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANE 179
Cdd:pfam02878 79 TPAVSFATRKLKADG-----GIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
42-521 |
1.40e-32 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 129.94 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 42 FGTSGHRGSAGRhNFNEQHILAIAQAIAENRAKNGITgpcyVGKDTHAlSEPAFIS-VLEVLAANGVDVIvqeNNGFTPT 120
Cdd:TIGR03990 4 FGTSGIRGIVGE-ELTPELALKVGKAFGTYLRGGKVV----VGRDTRT-SGPMLENaVIAGLLSTGCDVV---DLGIAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 121 PAVSNAILVHNKKGGpladgIVITPSHNPPEDGGIKynppnggpadtnvtkVVENRANELLAAGLQGVKRI--SLDAALA 198
Cdd:TIGR03990 75 PTLQYAVRELGADGG-----IMITASHNPPEYNGIK---------------LLNSDGTELSREQEEEIEEIaeSGDFERA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 199 S----GHVKEQ-DLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSG----IEYWKRIGehykLDLTIVNDQVDQTFrfm 269
Cdd:TIGR03990 135 DwdeiGTVTSDeDAIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAGslttPYLLRELG----CKVITLNCQPDGTF--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 270 hldkdgAIRMdcsSECAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRpqwGKDV 343
Cdd:TIGR03990 208 ------PGRN---PEPTPENLKDLSAlvkatGADLGIAHDGDADRLVFIDEKGrFIGGDYTLALFAKYLLEHG---GGKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 344 AVgkTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDGTPwstdkDGIIMCLLAAEITA 423
Cdd:TIGR03990 276 VT--NVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGNGGWIFPDHHYCR-----DGLMAAALFLELLA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 424 VTGKNPQEhyneLAERFgaPSYNRLQASATSAQKAALSKLspEMVSADTLAGDPITarltaapgngasIGGLKVMTDNGW 503
Cdd:TIGR03990 349 EEGKPLSE----LLAEL--PKYPMSKEKVELPDEDKEEVM--EAVEEEFADAEIDT------------IDGVRIDFEDGW 408
|
490
....*....|....*...
gi 505180591 504 FAARPSGTEDAYKIYCES 521
Cdd:TIGR03990 409 VLVRPSGTEPIVRIYAEA 426
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
42-539 |
4.00e-28 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 116.90 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 42 FGTSGHRGSAGRhNFNEQHILAIAQAIAENRAKngitGPCYVGKDTHAlSEPAFISVLE-VLAANGVDVIVQennGFTPT 120
Cdd:cd03087 2 FGTSGIRGVVGE-ELTPELALKVGKALGTYLGG----GTVVVGRDTRT-SGPMLKNAVIaGLLSAGCDVIDI---GIVPT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 121 PAVSNAILVHNKKGgpladgIVITPSHNPPEDGGIKYNPPNGgpadTNVTKVVENRANELLAAGlqGVKRISLDaalASG 200
Cdd:cd03087 73 PALQYAVRKLGDAG------VMITASHNPPEYNGIKLVNPDG----TEFSREQEEEIEEIIFSE--RFRRVAWD---EVG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 201 HVKEQD-LVQPFIEGLADIVDMAAiqKAGLKLGVDPLGGSG----IEYWKRIGehykLDLTIVNDQVDQTFrfmhldkdg 275
Cdd:cd03087 138 SVRREDsAIDEYIEAILDKVDIDG--GKGLKVVVDCGNGAGslttPYLLRELG----CKVITLNANPDGFF--------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 276 AIRMdcsSECAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRpqwGKDVAVgkTL 349
Cdd:cd03087 203 PGRP---PEPTPENLSELMElvratGADLGIAHDGDADRAVFVDEKGrFIDGDKLLALLAKYLLEEG---GGKVVT--PV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 350 VSSAMIDRVVNDLGRKLVEVPVGfKWFVDGLFDGSFG-FGGEESAGASFLRFDGTPwstdkDGIIMCLLAAEITAVTGKn 428
Cdd:cd03087 275 DASMLVEDVVEEAGGEVIRTPVG-DVHVAEEMIENGAvFGGEPNGGWIFPDHQLCR-----DGIMTAALLLELLAEEKP- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 429 pqehyneLAERFGA-PSYNRLQAS-ATSAQKAAlsklspEMVSAdtlagdpITARLTAAPGNGASIGGLKVMTDNGWFAA 506
Cdd:cd03087 348 -------LSELLDElPKYPLLREKvECPDEKKE------EVMEA-------VEEELSDADEDVDTIDGVRIEYEDGWVLI 407
|
490 500 510
....*....|....*....|....*....|...
gi 505180591 507 RPSGTEDAYKIYCESfLGEEHRKLIEKEAVEIV 539
Cdd:cd03087 408 RPSGTEPKIRITAEA-KTEERAKELLEEGRSKV 439
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
41-447 |
2.07e-22 |
|
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose 1,6-diphosphate intermediate, an important metabolic step in prokaryotes and eukaryotes. In one direction, G-1-P produced from sucrose catabolism is converted to G-6-P, the first intermediate in glycolysis. In the other direction, conversion of G-6-P to G-1-P generates a substrate for synthesis of UDP-glucose which is required for synthesis of a variety of cellular constituents including cell wall polymers and glycoproteins. The PGM1 family also includes a non-enzymatic PGM-related protein (PGM-RP) thought to play a structural role in eukaryotes, as well as pp63/parafusin, a phosphoglycoprotein that plays an important role in calcium-regulated exocytosis in ciliated protozoans. PGM1 belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100087 [Multi-domain] Cd Length: 548 Bit Score: 100.76 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 41 KFGTSGHRGSAG---RHNFNEQHILAIAQAIAENRAKNGITGpcyVGKDTHALSEPAFISVLEVLAANGVDVIVQENNGF 117
Cdd:cd03085 12 KPGTSGLRKKVKvfqQPNYLENFVQSIFNALPPEKLKGATLV---VGGDGRYYNKEAIQIIIKIAAANGVGKVVVGQNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 118 TPTPAVSNAILVHNKKGGpladgIVITPSHNP--PE-DGGIKYNPPNGGPADTNVT-------------KVVENRANELL 181
Cdd:cd03085 89 LSTPAVSAVIRKRKATGG-----IILTASHNPggPEgDFGIKYNTSNGGPAPESVTdkiyeitkkiteyKIADDPDVDLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 182 AAGLQGVKRISLDaalasghVKEQDLVQPFIEGLADIVDMAAIQKA----GLKLGVDPLGGSGIEYWKRI-GEHYKLDL- 255
Cdd:cd03085 164 KIGVTKFGGKPFT-------VEVIDSVEDYVELMKEIFDFDAIKKLlsrkGFKVRFDAMHGVTGPYAKKIfVEELGAPEs 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 256 TIVNDQVDQTFRFMHLD------KDGAIRMDcssecamagllalRDKFDLAFANDPDYDRHGIVTPAGLMNPNHYLAV-- 327
Cdd:cd03085 237 SVVNCTPLPDFGGGHPDpnltyaKDLVELMK-------------SGEPDFGAASDGDGDRNMILGKGFFVTPSDSVAVia 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 328 ----AINYLFQHRPQwgkdvAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDgLFD-GSFGFGGEESAGAsflrfdG 402
Cdd:cd03085 304 anakLIPYFYKGGLK-----GVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGN-LMDaGKLSLCGEESFGT------G 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 505180591 403 TPWSTDKDGI--IMCLLAaeITAVTGKNPQEHYNELAERFGAPSYNR 447
Cdd:cd03085 372 SDHIREKDGLwaVLAWLS--ILAHRNVSVEDIVKEHWQKYGRNFYTR 416
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
41-412 |
2.00e-20 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 94.72 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 41 KFGTSGHRGSAG---RHNFNEQHILAIAQAIAENRAKNGITGpcyVGKDTHALSEPAFISVLEVLAANGVDVIVQENNGF 117
Cdd:PLN02307 24 KPGTSGLRKKVKvfmQENYLANFVQALFNALPAEKVKGATLV---LGGDGRYFNKEAIQIIIKIAAANGVRRVWVGQNGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 118 TPTPAVSNAIlvHNKKGGPLADGIVITPSHNP--P-EDGGIKYNPPNGGPADTNVT-KVVEN--RANELLAAglQGVKRI 191
Cdd:PLN02307 101 LSTPAVSAVI--RERDGSKANGGFILTASHNPggPeEDFGIKYNYESGQPAPESITdKIYGNtlTIKEYKMA--EDIPDV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 192 SLDAALASGH-------VKEQDLVQPFIEGLADIVDMAAIQK----AGLKLGVDPLGGSGIEYWKRI------------- 247
Cdd:PLN02307 177 DLSAVGVTKFggpedfdVEVIDPVEDYVKLMKSIFDFELIKKllsrPDFTFCFDAMHGVTGAYAKRIfveelgapessll 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 248 ---------GEHYKLDLTIVNDQVDQtfrfMHLDKDGAIrmdcssecamagllalRDKFDLAFANDPDYDRHGIVTPAGL 318
Cdd:PLN02307 257 ncvpkedfgGGHPDPNLTYAKELVKR----MGLGKTSYG----------------DEPPEFGAASDGDGDRNMILGKRFF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 319 MNPNHYLAV-------AINYlFQHRPQwgkdvAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEE 391
Cdd:PLN02307 317 VTPSDSVAIiaanaqeAIPY-FSGGLK-----GVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKLSICGEE 390
|
410 420
....*....|....*....|.
gi 505180591 392 SAGAsflrfdGTPWSTDKDGI 412
Cdd:PLN02307 391 SFGT------GSDHIREKDGI 405
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
48-512 |
8.40e-20 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 92.19 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 48 RGSAGRhNFNEQHILAIAQAIAEnRAKNGITGPCYVGKDTHaLSEPAFISVL-EVLAANGVDVIvqeNNGFTPTPAVSNA 126
Cdd:cd03089 8 RGIAGE-ELTEEIAYAIGRAFGS-WLLEKGAKKVVVGRDGR-LSSPELAAALiEGLLAAGCDVI---DIGLVPTPVLYFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 127 IlVHNKKGGpladGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEnRANELLAAGLQGvkrisldaalaSGHVKEQD 206
Cdd:cd03089 82 T-FHLDADG----GVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRE-RAEKGDFAAATG-----------RGSVEKVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 207 LVQPFIEGLADIVDmaaIQKAGLKLGVDPLGGSGIEYWKRIGEHYKLDLTIVNDQVDQTFRFMHLDKdgairmdcSSECA 286
Cdd:cd03089 145 ILPDYIDRLLSDIK---LGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDP--------TDPEN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 287 MAGLLA--LRDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPqwGKDVaVGKTLVSSAMIDrVVNDLG 363
Cdd:cd03089 214 LEDLIAavKENGADLGIAFDGDGDRLGVVDEKGeIIWGDRLLALFARDILKRNP--GATI-VYDVKCSRNLYD-FIEEAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 364 RKLVEVPVGFKWFVDGLFDGSFGFGGEESA----GASFLRFDgtpwstdkDGIIMCLLAAEITAVTGKNPQEHYNELAER 439
Cdd:cd03089 290 GKPIMWKTGHSFIKAKMKETGALLAGEMSGhiffKDRWYGFD--------DGIYAALRLLELLSKSGKTLSELLADLPKY 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180591 440 FGAPSYNRlqASATSAQKAALSKLSpemVSADTLAGDPITarltaapgngasIGGLKVMTDNGWFAARPSGTE 512
Cdd:cd03089 362 FSTPEIRI--PVTEEDKFAVIERLK---EHFEFPGAEIID------------IDGVRVDFEDGWGLVRASNTE 417
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
210-317 |
8.74e-19 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 81.57 E-value: 8.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 210 PFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIGEHYKLDLTIVNDQVDQTFRFmhldkdGAIRMDCSSECAMAG 289
Cdd:pfam02879 1 AYIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPT------RAPNPEEPEALALLI 74
|
90 100
....*....|....*....|....*...
gi 505180591 290 LLALRDKFDLAFANDPDYDRHGIVTPAG 317
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVVDERG 102
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
59-533 |
1.75e-14 |
|
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100096 Cd Length: 445 Bit Score: 75.81 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 59 QHILAIAQAIAENRAKngitGPCYVGKDTHALSEPAFISVLEVLAANGVDVIvqeNNGFTPTPAVSnaILVHNKKGgplA 138
Cdd:cd05803 22 RYVAAFATWQPERTKG----GKIVVGRDGRPSGPMLEKIVIGALLACGCDVI---DLGIAPTPTVQ--VLVRQSQA---S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 139 DGIVITPSHNPPEDGGIKYNPPNG---GPADtnVTKVVE-NRANELLAAGLQGVKRI-SLDAALASgHVKEqdlvqpfIE 213
Cdd:cd05803 90 GGIIITASHNPPQWNGLKFIGPDGeflTPDE--GEEVLScAEAGSAQKAGYDQLGEVtFSEDAIAE-HIDK-------VL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 214 GLADiVDMAAIQKAGLKLGVDPLGGSGIEYWKRIGEHYKLDLTIVNDQVDQTFR------------FMHLDKDgairmdc 281
Cdd:cd05803 160 ALVD-VDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFPhtpeplpenltqLCAAVKE------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 282 ssecamagllalrDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPQWGKDVavgKTLVSSAMIDRVVN 360
Cdd:cd05803 232 -------------SGADVGFAVDPDADRLALVDEDGrPIGEEYTLALAVDYVLKYGGRKGPVV---VNLSTSRALEDIAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 361 DLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAG-----ASFLRfdgtpwstdkDGIIMCLLAAEITAVTGKNPQEHYNE 435
Cdd:cd05803 296 KHGVPVFRSAVGEANVVEKMKEVDAVIGGEGNGGvilpdVHYGR----------DSLVGIALVLQLLAASGKPLSEIVDE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 436 LaerfgaPSYnrlqasATSAQKAALSKLSPEmVSADTLAGDPITARLTaapgngaSIGGLKVMTDNGWFAARPSGTEDAY 515
Cdd:cd05803 366 L------PQY------YISKTKVTIAGEALE-RLLKKLEAYFKDAEAS-------TLDGLRLDSEDSWVHVRPSNTEPIV 425
|
490
....*....|....*...
gi 505180591 516 KIYCESFLGEEHRKLIEK 533
Cdd:cd05803 426 RIIAEAPTQDEAEALADR 443
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
42-156 |
2.22e-13 |
|
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100095 Cd Length: 434 Bit Score: 72.13 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 42 FGTSGHRGSAGRhNFNEQHILAIAQAIAENRAKNGITGPCYVGKDTHaLSEPAFISVLEV-LAANGVDVIVQennGFTPT 120
Cdd:cd05802 2 FGTDGIRGVANE-PLTPELALKLGRAAGKVLGKGGGRPKVLIGKDTR-ISGYMLESALAAgLTSAGVDVLLL---GVIPT 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 505180591 121 PAVsnAILVHNKKggplAD-GIVITPSHNPPEDGGIK 156
Cdd:cd05802 77 PAV--AYLTRKLR----ADaGVVISASHNPFEDNGIK 107
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
41-162 |
1.47e-05 |
|
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose 6-phosphate to mannose-1-phosphate in the second of three steps in the GDP-mannose pathway, in which GDP-D-mannose is synthesized from fructose-6-phosphate. In Mycobacterium tuberculosis, the causative agent of tuberculosis, PMM is involved in the biosynthesis of mannosylated lipoglycans that participate in the association of mycobacteria with host macrophage phagocytic receptors. ManB belongs to the the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100090 Cd Length: 459 Bit Score: 47.58 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 41 KFGTSGHRG--SAGRHNFNEQHILAIAQAIAENRAKNGItgpcYVGKDTHAlSEPAF-ISVLEVLAANGVDVIvqeNNGF 117
Cdd:cd03088 1 KFGTSGLRGlvTDLTDEVCYAYTRAFLQHLESKFPGDTV----AVGRDLRP-SSPRIaAACAAALRDAGFRVV---DCGA 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 505180591 118 TPTPAVSNAILVHNkkggplADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:cd03088 73 VPTPALALYAMKRG------APAIMVTGSHIPADRNGLKFYRPDG 111
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
42-162 |
2.77e-05 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 46.67 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 42 FGTSGHRGSAGRHNFNEQHIL----AIAQAIAENRAKNGItgpcyVGKDTHaLSEPAFISVLEV-LAANGVDVivqennG 116
Cdd:PRK10887 4 FGTDGIRGKVGQAPITPDFVLklgwAAGKVLARQGRPKVL-----IGKDTR-ISGYMLESALEAgLAAAGVDV------L 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 505180591 117 FT---PTPAVsnAILVHNKKggpLADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:PRK10887 72 LTgpmPTPAV--AYLTRTLR---AEAGIVISASHNPYYDNGIKFFSADG 115
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
140-163 |
2.03e-04 |
|
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100088 Cd Length: 513 Bit Score: 44.12 E-value: 2.03e-04
10 20
....*....|....*....|....
gi 505180591 140 GIVITPSHNPPEDGGIKYNPPNGG 163
Cdd:cd03086 38 GVMITASHNPVEDNGVKIVDPDGE 61
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
140-178 |
3.59e-04 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 43.49 E-value: 3.59e-04
10 20 30
....*....|....*....|....*....|....*....
gi 505180591 140 GIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRAN 178
Cdd:PTZ00302 78 GVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFAN 116
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
489-535 |
1.80e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 37.25 E-value: 1.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 505180591 489 GASIGGLKVMTDNGW-FAARPSGTEDAYKIYCESFLGEEHRKLIEKEA 535
Cdd:pfam00408 20 KVFADAEKILGEDGRrLDVRPSGTEPVLRVMVEGDSDEELARLADEIA 67
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
140-202 |
9.74e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 38.85 E-value: 9.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180591 140 GIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRAN-----ELLAAGLQGVKR--ISLDAALASGHV 202
Cdd:PLN02895 61 GLMITASHNPVSDNGVKIVDPSGGMLPQAWEPFADALANapdpdALVQLIREFVKKenIPAVGGNPPAEV 130
|
|
| |
